Funds for the purchase of a Bruker ElexSys E680 FT/CW spectrometer are requested. The spectrometer will seed the establishment of an advanced electron spin resonance (ESR) facility at Pitt, and will initially serve a group of nine investigators (Curran, Jen-Jacobson, Klein- Seetharaman, Saxena, Schafmeister, Trakselis, Waldeck, Wetzel, and Wipf). Seven of the users are supported by NIH grant types including P01, P50, R01, and R37 (MERIT). The primary appointments of the investigators are in Chemistry (Curran, Saxena, Trakselis, Waldeck, Wipf), Biology (Jen- Jacobson) and in the Medical School (Klein-Seetharaman, Wetzel) at the University of Pittsburgh, and in Chemistry (Schafmeister) at Temple University. Several of these investigators work collaboratively on the elucidation of structure-function relationships in membrane proteins and oligomeric proteins. The microscopic origins of macroscopic behavior of many of these systems cannot be easily understood using conventional structural tools, such as nuclear magnetic resonance or X-Ray diffraction. The spectrometer will be used to determine protein structure and dynamics, as well as electron transfer processes in chemical and biological materials. The high frequency spectrometer will: (a) allow sensitive measurement of fast dynamics in proteins and macromolecules;(b) enable high resolution measurement of nanometer range distances in biomolecules in order to determine constraints on macromolecular structure and conformational dynamics;(c) allow measurement of electron-nuclear distances in order to reveal metal-ion coordination in macromolecules;(d) monitor electron transfer and charge transfer processes in chemical and biological materials;and (e) enable enhanced resolution to the identity of transient radicals in order to elucidate organic reaction mechanisms. The user group requires more capacity for high-end pulsed ESR experiments, access to high frequency ESR experiments, as well as more sensitivity for concentration limited samples - these needs dictate the requested instrument. The Department of Chemistry will provide $175,000 as matching funds for the purchase of the spectrometer, as well as renovate and configure suitable space for the spectrometer in the Chevron Science Center (Chemistry Department). Biomedical Relevance: The spectrometer will support several projects that have strong biomedical relevance. These include the measurement of structure and conformational dynamics of several membrane proteins that are attractive drug targets, misfolding of several proteins implicated in neurodegenerative diseases, establishment of the general principles of protein-DNA interaction, as well as innovative synthetic chemistry directed towards drug discovery.